| abstract |
A process is provided for cleaving a polypeptide into at lease two polypeptide components comprising treating a reduced, free-cysteine form of the polypeptide with a cleaving agent under conditions for cleaving the polypeptide at a desired junction between the polypeptide cleavage products. More preferably, the process for cleaving comprises culturing cells containing DNA encoding said polypeptide, wherein at least one Asp codon is present in said DNA at a desired junction between the components to be cleaved from each other, said culturing resulting in expression of the DNA to produce the polypeptide in the host cell culture; and treating a reduced, free-cysteine form of the polypeptide with dilute acid under conditions for cleaving the polypeptide at the Asp junction. In particular embodiments, a DNA sequence is provided that encodes a relaxin precursor and includes codons encoding aspartic acid-containing linkers at novel positions within the precursor, allowing the ready cleavage of relaxin A peptides by treatment with dilute acid. |